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Literature summary extracted from

  • Hayman, M.W.; Fawcett, T.; Slabas, A.R.
    Kinetic mechanism and order of substrate binding for sn-glycerol-3-phosphate acyltransferase from squash (Cucurbita moschata) (2002), FEBS Lett., 514, 281-284.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.15 expression of N-terminal truncated enzyme in Escherichia coli, overexpression of wild-type acyltransferase in tobacco Cucurbita moschata
2.3.1.15 overexpression in tobacco Arabidopsis thaliana

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.15 0.003 0.0034 acyl-ACP recombinant N-terminal truncated acyltransferase Cucurbita moschata

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.15 Arabidopsis thaliana
-
-
-
2.3.1.15 Cucurbita moschata
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.15 an acyl-CoA + sn-glycerol 3-phosphate = CoA + a 1-acyl-sn-glycerol 3-phosphate reaction proceeds via a compulsory-ordered ternary with acyl-ACP binding before glycerol 3-phosphate Cucurbita moschata
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.15 acyl-CoA + sn-glycerol 3-phosphate very low activity with butanoyl-CoA and hexanoyl-CoA Cucurbita moschata CoA + 1-acyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.15 acyl-[acyl-carrier protein] + sn-glycerol 3-phosphate
-
 Cucurbita moschata acyl-carrier protein + 1-acyl-sn-glycerol 3-phosphate
-
 ?